Protein

UniProt accession
A4K487 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MVRYIPAAHHSAGSNNPVNRVVIHATCPDVGFPSASRKGRAVSTANYFASPSSGGSAHYVCDIGETVQCLSESTIGWHAPPNPHSLGIEICADGGSHASFRVPGHAYTREQWLDPQVWPAVERAAVLCRRLCDKYNVPKRKLSAADLKAGRRGVCGHVDVTDAWHQSDHDDPGPWFPWDKFMAVVNGGSGDSGELTVADVKALHDQIKQLSAQLTGSVNKLHHDVGVVQVQNGDLGKRVDALSWVKNPVTGKLWRTKDALWSVWYYVLECRSRLDRLESAVNDLKK
Physico‐chemical
properties
protein length:286 AA
molecular weight:31273,00000 Da
isoelectric point:8,38703
aromaticity:0,07692
hydropathy:-0,37308

Domains

Domains [InterPro]
IPR002502
7–173
IPR002502
IPR051206
16–248
IPR051206
IPR036505
1–192
IPR036505
IPR036505
6–182
IPR036505
IPR002502
15–174
IPR002502
IPR002502
17–175
IPR002502
Protein sequence: A4K487
1 286
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Propionibacterium phage PA6
[NCBI] 		376758 Pahexavirus > Pahexavirus PA6
Host Propionibacterium acnes
[NCBI] 		1747 Bacteria > Actinobacteria > Actinobacteria > Propionibacteriales > Propionibacteriaceae > Propionibacterium

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ABE68589.1 [NCBI]
Genbank nucleotide accession
DQ431235 [NCBI]
CDS location
range 15376 -> 16236
strand +
CDS
GTGGTGAGATACATTCCTGCAGCGCATCACTCTGCCGGCTCTAATAATCCGGTGAACAGGGTTGTGATTCATGCAACATGCCCGGATGTGGGGTTTCCGTCCGCCTCACGTAAGGGGCGGGCGGTGTCTACAGCAAACTATTTCGCTTCCCCATCGTCTGGTGGTTCGGCGCATTATGTGTGTGATATTGGGGAGACGGTGCAATGCTTGTCGGAGTCTACGATTGGTTGGCATGCCCCGCCGAATCCGCATTCTTTGGGTATCGAGATTTGCGCGGATGGGGGTTCGCATGCCTCGTTCCGTGTGCCGGGGCATGCTTACACTCGGGAGCAGTGGCTTGATCCGCAGGTGTGGCCTGCCGTTGAGAGGGCGGCGGTGCTGTGTAGACGTTTGTGTGACAAATATAATGTTCCGAAAAGGAAACTGTCGGCTGCCGATTTGAAGGCTGGCAGGCGGGGTGTGTGTGGCCATGTGGATGTTACGGATGCGTGGCATCAGTCGGATCATGACGATCCTGGGCCGTGGTTTCCGTGGGACAAATTTATGGCCGTCGTCAACGGCGGCAGTGGAGATAGTGGGGAGTTAACTGTGGCTGATGTGAAAGCCTTGCATGATCAGATTAAACAATTGTCTGCTCAGCTTACTGGTTCGGTGAATAAGCTGCACCATGATGTTGGTGTGGTTCAGGTTCAGAATGGTGATTTGGGTAAACGTGTTGATGCCTTGTCGTGGGTGAAGAATCCTGTGACGGGGAAGCTGTGGCGCACTAAGGATGCCCTGTGGAGTGTCTGGTATTACGTGTTGGAGTGTCGTAGCCGTCTTGACAGGCTCGAGTCTGCTGTCAACGATTTGAAAAAGTGA

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell Biological process Inferred from Electronic Annotation (InterPro)
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0009253 peptidoglycan catabolic process Biological process Inferred from Electronic Annotation (InterPro)
GO:0009254 peptidoglycan turnover Biological process Inferred from Electronic Annotation (TreeGrafter)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)
GO:0071555 cell wall organization Biological process Inferred from Electronic Annotation (UniProt)

Enzymatic activity

EC Number Entry Name Reaction Catalyzed Classification Evidence Source
3.5.1.28 N-acetylmuramoyl-L-alanine amidase residues in certain cell-wall glycopeptides
Hydrolases
Acting on carbon-nitrogen bonds, other than peptide bonds
In linear amides
 match to sequence model evidence used in automatic assertion
ECO:0000256 		ARBA:ARBA00001561

Tertiary structure

No tertiary structures available.